ID E5R1R5_ARTGP Unreviewed; 1670 AA.
AC E5R1R5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=MGYG_01576 {ECO:0000313|EMBL:EFQ98549.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; DS989822; EFQ98549.1; -; Genomic_DNA.
DR RefSeq; XP_003177501.1; XM_003177453.1.
DR STRING; 535722.E5R1R5; -.
DR GeneID; 10032831; -.
DR VEuPathDB; FungiDB:MGYG_01576; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_001837_3_1_1; -.
DR InParanoid; E5R1R5; -.
DR OMA; CHWIGKG; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF401; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1670
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003197838"
FT DOMAIN 114..157
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 173..537
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DISULFID 128..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 133..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 151..155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1670 AA; 183794 MW; 933DD3828596625A CRC64;
MALTAKANRN LRPLSLFFLA TALFFLCKLS EAAIHGEAAV PGSNVPGANF TEIDIYQSSS
FVQFAKKGTD YSCRKGVPCK NNACCGSFMG TNTGICGFGD AFCGGDCDSK CDAKAECGKY
ADPPGKECPL KVCCSKYGFC GSSAEFCGTG CQSNCIEKPP LPPGGSAMSV LGNKIIGYYE
AWADRRTCRE FPPSSIPVQG LTHVNFAFAY VDPDSLTITA MDSSTPASLF SQVTDIKNMK
SRSSTLEVYI SLGGWTFSDN GTSTQSVFPS IAADPEKRQK FADNLVTFMR HYGFDGVDLD
WEYPGAPDRG GNGKEDIPNY VALLKTLRQT FKASARGNYG LSFTIPTSYW YLKWFDVPGL
LQYADWVNLM TYDLHGVWDQ HNPIGNIVQG HTNLTEIQAA FDLLWRNNVP PGKVVMGVGF
YGRSFQLKDR TCAHPGCEFS GPANAGSCTK SAGTLAYFEI MDIIKNEKPE VVHDAEAAVN
YFAYGDQKDQ WISYDDSKTL QQKVKWADSK GLGGVLVWSV DQDDNSFSAL EGLIGEPLPA
FSEKLKRHTI DDAGHWSSTN GQACRVSECV KVDTDPPSGY TVAPNGKFPD TCSGGEYKYV
WCPTHSMPDS CEWRGSGSCH GQCHPGEVTL AHSPHGSLSC LRPGQQAFCC VSSTWAKHVE
KCRWGEPHKD CPSDVPYALS TKNSFPKYTQ EHFCCPFKFE NCHWVGKGTC DDNECSSTDV
QVALDPVGDG SAECFSSDRR KPLCCNPPAN VNPFLPVPLE DLFPTLPPLT NIPAFDLQPI
SYVSSLATDK NDPSTFFLVV IDGPPGTVSN ANKRDGSDLE FVSGAVHHGQ SPQTAHFVCM
NNSSKSNCND MHSDGLEGTI LRMPDGMGFA KYAVAHSVKE SNFSVPRYLA KRAPIDAKVF
ELEYSYNFSK AKRGDEPIYF RVDYSDTDNY YTEVVKGHHQ KRNLGRRFWS SSKSVWKNLF
KRLRGQVYNA LTQPSLSYEN FNTLIYGNDG KKKGCKGADG FLKLNLSGSM RNVMQFGFTI
IGTMHPFAID EAYGFYDSSL HMSGKLEFDG KGELSINEGV GVSRKLLRSS ITKYEASHPG
LVSFSPSMNA DISLVGSGYM DGRFTANFEV DWGLGTHAPP DMGKFYGYSI SPKPSNPSGY
ISVKEATYND LFSMNINLET TMELNLFDYK TSEQNAKALF TARVPHAIRV VGNVGSGNPA
VINSPQQATS EVIQTGIQSG WDDGTTHLLG HRYDSYVLFS GGEAPVGARE TPEINGYALF
GDKDFMSCSE PADNLTCTFS LAENDPSYSQ PSLENQLEFE LKQSFLESLS DKERALYNDT
LSKRAGPSSG HANTYAIYDW PDTGNNYAFN FETPTYPNGG NGAALDAETG RNERYSLANP
TDCVDTSITA NGVLGTNYMT VETEHPFDRT IFPTHFANFI QRGVLDLDDR FGTRAFTTNL
PTWEWEQLYD TFAHDYRIWV PRGRGINIPP GTPSADVANA LGSTSNPGVL SNLERDLNAS
CPPLLLSVQR ANVLVWKLQN LKGRVYTTSG DPTSDDVWDG WMTATATNAN IALSSLRAIF
AVFNYMNAIS SDRAAVLEDI TATLEQFDEI YGQVYPTRPE RLAPLWAEFQ TQWNIRVVYH
ATSYLTRRLD SLYNLWNPLT MTVNPLRTAA VLIVTKIRTL RAKIPTEIRL
//
